6ee0: Difference between revisions
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==Crystal Structure of SNX23 PX domain== | ==Crystal Structure of SNX23 PX domain== | ||
<StructureSection load='6ee0' size='340' side='right' caption='[[6ee0]], [[Resolution|resolution]] 2.52Å' scene=''> | <StructureSection load='6ee0' size='340' side='right'caption='[[6ee0]], [[Resolution|resolution]] 2.52Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6ee0]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EE0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EE0 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6ee0]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EE0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EE0 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ee0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ee0 OCA], [http://pdbe.org/6ee0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ee0 RCSB], [http://www.ebi.ac.uk/pdbsum/6ee0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ee0 ProSAT]</span></td></tr> | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KIF16B, C20orf23, KIAA1590, SNX23 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ee0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ee0 OCA], [http://pdbe.org/6ee0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ee0 RCSB], [http://www.ebi.ac.uk/pdbsum/6ee0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ee0 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/KI16B_HUMAN KI16B_HUMAN]] Plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. Regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). Regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development.<ref>PMID:15882625</ref> | [[http://www.uniprot.org/uniprot/KI16B_HUMAN KI16B_HUMAN]] Plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. Regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). Regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development.<ref>PMID:15882625</ref> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Phox homology (PX) domains are membrane interacting domains that bind to phosphatidylinositol phospholipids or phosphoinositides, markers of organelle identity in the endocytic system. Although many PX domains bind the canonical endosome-enriched lipid PtdIns3P, others interact with alternative phosphoinositides, and a precise understanding of how these specificities arise has remained elusive. Here we systematically screen all human PX domains for their phospholipid preferences using liposome binding assays, biolayer interferometry and isothermal titration calorimetry. These analyses define four distinct classes of human PX domains that either bind specifically to PtdIns3P, non-specifically to various di- and tri-phosphorylated phosphoinositides, bind both PtdIns3P and other phosphoinositides, or associate with none of the lipids tested. A comprehensive evaluation of PX domain structures reveals two distinct binding sites that explain these specificities, providing a basis for defining and predicting the functional membrane interactions of the entire PX domain protein family. | |||
Classification of the human phox homology (PX) domains based on their phosphoinositide binding specificities.,Chandra M, Chin YK, Mas C, Feathers JR, Paul B, Datta S, Chen KE, Jia X, Yang Z, Norwood SJ, Mohanty B, Bugarcic A, Teasdale RD, Henne WM, Mobli M, Collins BM Nat Commun. 2019 Apr 4;10(1):1528. doi: 10.1038/s41467-019-09355-y. PMID:30948714<ref>PMID:30948714</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6ee0" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Sorting nexin|Sorting nexin]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | |||
[[Category: Large Structures]] | |||
[[Category: Chandra, M]] | [[Category: Chandra, M]] | ||
[[Category: Collins, B M]] | [[Category: Collins, B M]] | ||
Revision as of 09:47, 17 April 2019
Crystal Structure of SNX23 PX domainCrystal Structure of SNX23 PX domain
Structural highlights
Function[KI16B_HUMAN] Plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. Regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). Regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development.[1] Publication Abstract from PubMedPhox homology (PX) domains are membrane interacting domains that bind to phosphatidylinositol phospholipids or phosphoinositides, markers of organelle identity in the endocytic system. Although many PX domains bind the canonical endosome-enriched lipid PtdIns3P, others interact with alternative phosphoinositides, and a precise understanding of how these specificities arise has remained elusive. Here we systematically screen all human PX domains for their phospholipid preferences using liposome binding assays, biolayer interferometry and isothermal titration calorimetry. These analyses define four distinct classes of human PX domains that either bind specifically to PtdIns3P, non-specifically to various di- and tri-phosphorylated phosphoinositides, bind both PtdIns3P and other phosphoinositides, or associate with none of the lipids tested. A comprehensive evaluation of PX domain structures reveals two distinct binding sites that explain these specificities, providing a basis for defining and predicting the functional membrane interactions of the entire PX domain protein family. Classification of the human phox homology (PX) domains based on their phosphoinositide binding specificities.,Chandra M, Chin YK, Mas C, Feathers JR, Paul B, Datta S, Chen KE, Jia X, Yang Z, Norwood SJ, Mohanty B, Bugarcic A, Teasdale RD, Henne WM, Mobli M, Collins BM Nat Commun. 2019 Apr 4;10(1):1528. doi: 10.1038/s41467-019-09355-y. PMID:30948714[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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